Cloned (Comment) | Organism |
---|---|
cloned and overexpressed | Pseudomonas aeruginosa |
Crystallization (Comment) | Organism |
---|---|
1.8 A resolution. PvdQ has a typical alpha/beta heterodimeric Ntn-hydrolase fold. It has a large, hydrophobic binding pocket, ideally suited to recognize C12 fatty acid-like chains of N-acylhomoserine lactones. Binding of a C12 fatty acid or a 3-oxo-C12 fatty acid induces subtle conformational changes to accommodate the aliphatic chain. PvdQ is the first structurally characterized Ntn-hydrolase within this family to have any disulfide bridges. The disulfides are located in both the alpha- and beta-chain on the periphery of the protein | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | Q9I194 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-3-oxodecanoyl-L-homoserine lactone + H2O | - |
Pseudomonas aeruginosa | L-homoserine lactone + 3-oxodecanoic acid | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AHL acylase | - |
Pseudomonas aeruginosa |
PvdQ | - |
Pseudomonas aeruginosa |
quorum-quenching N-acyl homoserine lactone acylase PvdQ | - |
Pseudomonas aeruginosa |